IgY‐binding peptide screened from a random peptide library as a ligand for IgY purification

Khan, Kamrul Hasan; Himeno, Arisa; Kosugi, Shouhei; Nakashima, Y.; Rafique, Abdur; Imamura, Ayana; Hatanaka, Takaaki; Kato, Dai‐ichiro; Ito, Yuji

doi:10.1002/psc.3027

Cited by 12 publications

(7 citation statements)

References 20 publications

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“…IgY is the major low molecular weight immunoglobulin in oviparous animals (41). This type of antibody has distinctive properties, explored in various ways in research, diagnostics, and therapy.…”

Section: Discussionmentioning

confidence: 99%

Evaluation of Human Anti Igg Polyclonal Antibody Production Conjugated with Peroxidase in Egg Yolk

Abdolmaleki¹,

Zamani²,

Talebi³

2020

ijph

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Background: Egg yolk is a rich and accessible source of yolk immunoglobulin (Y immunoglobulin). Presently, polyclonal antibodies from mammalian sources are used for diagnosis. Antibody production from egg yolk gives a higher yield and turnover than that from lab animals, and invasive methods such as phlebotomy and causing stress to the animals are not required. Due to the issues regarding mammalian antibodies, we aimed to evaluate the human anti-IgG polyclonal antibody production conjugated with peroxidase in egg yolk.Methods: Population of laying hens reared in Agriculture/Isfahan University of Technology were used in 2017. After immunizing hen against pure human IgG, specific IgY (yolk immunoglobulin) was purified from the yolk by sedimentation with polyethylene glycol (PEG6000). To assess the molecular weight and activity of the product, SDS-PAGE and ELISA-test were used, respectively.Results: The complete molecular weight of IgY was 180 kDa and the molecular weight of its light and heavy chains were 27 and 67 kDa, respectively.Conclusion: Antihuman IgG IgY had a purity above 90%. The product of this study can be used to measure IgG class antibodies in order to diagnose different diseases.

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Section: Discussionmentioning

confidence: 99%

Evaluation of Human Anti Igg Polyclonal Antibody Production Conjugated with Peroxidase in Egg Yolk

Abdolmaleki¹,

Zamani²,

Talebi³

2020

ijph

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“…Other types of ligands are therefore required, such as the elastin-like polypeptide-tagged immunoglobulin-binding domain of streptococcal protein G[ 67 ]. Still other ligands, such as IgY-binding peptides screened from a random peptide library, have been also proposed as a means of IgY purification[ 68 ]. IgY can also be purified with thiophilic adsorption chromatography, usually through commercially available IgY-extraction columns[ 18 , 69 ].…”

Section: Development and Evaluation Of Egg Yolk-derived Polyclonal Igysmentioning

confidence: 99%

IgY technology: Methods for developing and evaluating avian immunoglobulins for the in vitro detection of biomolecules

Karachaliou¹,

Vassilakopoulou²,

Livaniou³

2021

WJM

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The term “IgY technology” was introduced in the literature in the mid 1990s to describe a procedure involving immunization of avian species, mainly laying hens and consequent isolation of the polyclonal IgYs from the “immune” egg yolk (thus avoiding bleeding and animal stress). IgYs have been applied to various fields of medicine and biotechnology. The present article will deal with specific aspects of IgY technology, focusing on the currently reported methods for developing, isolating, evaluating and storing polyclonal IgYs. Other topics such as current information on isolation protocols or evaluation of IgYs from different avian species are also discussed. Specific advantages of IgY technology ( e.g. , novel antibody specificities that may emerge via the avian immune system) will also be discussed. Recent in vitro applications of polyclonal egg yolk-derived IgYs to the field of disease diagnosis in human and veterinary medicine through in vitro immunodetection of target biomolecules will be presented. Moreover, ethical aspects associated with animal well-being as well as new promising approaches that are relevant to the original IgY technology ( e.g. , development of monoclonal IgYs and IgY-like antibodies through the phage display technique or in transgenic chickens) and future prospects in the area will also be mentioned.

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“…4 ). Many ligands for Ab purification have been developed by screening phage displayed libraries (Krook et al 1998 ; DeLano et al 2000 ; Ehrlich and Bailon 2001 ; Hatanaka et al 2012 ; Yoo and Choi 2015 ; Khan et al 2017 ). Similar biological libraries such as mRNA-display, yeast-display and ribosomal-display technologies has been also developed but most frequently applied in therapeutic drug development (Galán et al 2016 ).…”

Section: Peptide Libraries Synthesismentioning

confidence: 99%

“…Khan et al ( 2017 ), screening cyclic phage-display libraries, developed peptide ligands useful to purify chicken egg yolk immunoglobulin (IgY) by AC with a yield of 70%. However, oligomers of IgY were produced due to the low pH of the elution buffer.…”

Section: Examples Of Peptide Ligands Designed For Antibodies Purificationmentioning

confidence: 99%

Peptide Affinity Chromatography Applied to Therapeutic Antibodies Purification

Barredo-Vacchelli

Giudicessi

Martínez‐Ceron

et al. 2021

Int J Pept Res Ther

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The interest in therapeutic monoclonal antibodies (mAbs) has significantly grown in the pharmaceutical industry, exceeding 100 FDA mAbs approved. Although the upstream processing of their industrial production has been significantly improved in the last years, the downstream processing still depends on immobilized protein A affinity chromatography. The high cost, low capacity and short half-life of immobilized protein A chromatography matrices, encouraged the design of alternative short-peptide ligands for mAb purification. Most of these peptides have been obtained by screening combinatorial peptide libraries. These low-cost ligands can be easily produced by solid-phase peptide synthesis and can be immobilized on chromatographic supports, thus obtaining matrices with high capacity and selectivity. Furthermore, matrices with immobilized peptide ligands have longer half-life than those with protein A due to the higher stability of the peptides. In this review the design and synthesis of peptide ligands, their immobilization on chromatographic supports and the evaluation of the affinity supports for their application in mAb purification is described.

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IgY‐binding peptide screened from a random peptide library as a ligand for IgY purification

Cited by 12 publications

References 20 publications

Evaluation of Human Anti Igg Polyclonal Antibody Production Conjugated with Peroxidase in Egg Yolk

Evaluation of Human Anti Igg Polyclonal Antibody Production Conjugated with Peroxidase in Egg Yolk

IgY technology: Methods for developing and evaluating avian immunoglobulins for the in vitro detection of biomolecules

Peptide Affinity Chromatography Applied to Therapeutic Antibodies Purification

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